PURIFICATION OF CARBONIC-ANHYDRASE ISOENZYMES BY HIGH-PERFORMANCE AFFINITY-CHROMATOGRAPHY AND HYDROPHOBIC INTERACTION CHROMATOGRAPHY

被引：7

作者：

ABOUREBYEH, H

JOSIC, D

GOTTSCHALL, K

SCHUBERTREHBERG, K

KORBER, F

机构：

[1] SAULENTECH & EUROCHROM DR ING KNAUER GMBH,HEGAUER WEG 38,W-1000 BERLIN 37,GERMANY

[2] FREE UNIV BERLIN,INST MOLEK BIOL & BIOCHEM,W-1000 BERLIN 33,GERMANY

来源：

JOURNAL OF CHROMATOGRAPHY-BIOMEDICAL APPLICATIONS | 1991年 / 566卷 / 02期

关键词：

D O I：

10.1016/0378-4347(91)80251-7

中图分类号：

O65 [分析化学];

学科分类号：

070302 ; 081704 ;

摘要：

Isoenzymes of carbonic anhydrase were purified by a combination of affinity chromatography and hydrophobic interaction chromatography. Immobilization of sulfonamides on an epoxy-activated support provided a stationary phase for affinity chromatography which was stable to hydrolysis by carbonic anhydrase. A first purification step allowed the isolation of enzymes directly from homogenates of human erythrocytes and rat stomach. Without any further preparation, except the addition of ammonium sulfate to the eluate from affinity chromatography, the isoenzymes could be separated by hydrophobic interaction chromatography with very high recovery of protein and retention of enzymatic activity.

引用

页码：351 / 359

页数：9

共 16 条

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